Evidence that HDAC7 acts as an epigenetic "reader" of AR acetylation through NCoR-HDAC3 dissociation.
Evidence that HDAC7 acts as an epigenetic "reader" of AR acetylation through NCoR-HDAC3 dissociation.
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DOI：
10.1016/j.chembiol.2022.05.008
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发表时间：
2022-07-21
影响因子：
8.6
通讯作者：
Pflum, Mary Kay H.
中科院分区：
文献类型：
--
作者：
Zhang, Yuchen;Andrade, Rafael;Hanna, Anthony A.;Pflum, Mary Kay H.
Histone deacetylase (HDAC) proteins are epigenetic regulators that govern a wide variety of cellular events. With a role in cancer formation, HDAC inhibitors have emerged as anti-cancer therapeutics. Among the eleven metal-dependent class I, II and IV HDAC proteins targeted by inhibitor drugs, class IIa HDAC4, 5, 7, and 9 harbor low deacetylase activity and are hypothesized to be “reader” proteins, which bind to post-translationally acetylated lysine. However, evidence linking acetyllysine binding to a downstream functional event is lacking. Here, we report for the first time that HDAC4, 5 and 7 dissociated from corepressor NCoR in the presence of an acetyllysine-containing peptide, consistent with reader function. Documenting the biological consequences of this possible reader function, mutation of a critical acetylation site regulated Androgen Receptor (AR) transcriptional activation function through HDAC7-NCoR-HDAC3 dissociation. The data document the first evidence consistent with epigenetic reader functions of class IIa HDAC proteins. Zhang et al. report evidence for the epigenetic reader function of Histone Deacetylase 7 (HDAC7). A model is proposed where transcription by Androgen Receptor (AR) is activated by binding of the AR K630 acetylation site to HDAC7 and dissociation of the repressive NCoR-HDAC3 complex
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通讯作者：
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